Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Stephen G AddinallDavid I Roper

Abstract

An open reading frame designated b2910 (ygfE) in the Escherichia coli K12-MG1655 genome sequence, identified as a possible homologue to the cell-division protein ZapA, was cloned into the high-expression plasmid pETDuet-1 and overexpressed in E. coli BL21 (DE3)-AI. The protein was purified in three steps to 99% purity. Crystals were obtained by the hanging-drop vapour-diffusion method at 291 K from a wide range of screened conditions, but principally from solutions containing 0.1 M HEPES pH 7.0, 18% PEG 6000, 5 mM CaCl2. Diffraction data to 1.8 A were collected at the European Synchrotron Radiation Facility (ESRF). The crystals belong to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 53.8, b = 53.8, c = 329.7 A, alpha = beta = 90, gamma = 120 degrees.

References

Jan 1, 1997·Annual Review of Biochemistry·J Lutkenhaus, S G Addinall
Sep 9, 2000·FEMS Microbiology Reviews·W Margolin
Jun 8, 2002·Journal of Molecular Biology·Stephen G Addinall, Barry Holland
Oct 9, 2002·Genes & Development·Frederico J Gueiros-Filho, Richard Losick
Oct 7, 2003·Annual Review of Microbiology·Laura Romberg, Petra Anne Levin
Jan 27, 2004·Journal of Molecular Evolution·Sue VaughanStephen G Addinall
Aug 4, 2004·Journal of Molecular Biology·Harry H LowJan Löwe

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